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- PDB-7apw: The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-(benzo[d]t... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7apw | ||||||
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Title | The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-(benzo[d]thiazol-6-ylsulfonyl)-5-(methoxymethyl)-3-(pyridin-2-ylethyl)-3,10-diazabicyclo[4.3.1]decan-2-one | ||||||
![]() | Peptidyl-prolyl cis-trans isomerase FKBP5 | ||||||
![]() | CHAPERONE / Fk-506 binding domain / Hsp90 cochaperone / immunophiline / peptidyl-prolyl isomerase / ligand selectivity | ||||||
Function / homology | ![]() FK506 binding / chaperone-mediated protein folding / MECP2 regulates neuronal receptors and channels / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / ESR-mediated signaling / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / response to bacterium / protein folding ...FK506 binding / chaperone-mediated protein folding / MECP2 regulates neuronal receptors and channels / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / ESR-mediated signaling / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / response to bacterium / protein folding / protein-macromolecule adaptor activity / extracellular exosome / nucleoplasm / membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Voll, A.M. / Kolos, J.M. / Pomplun, S. / Riess, B. / Purder, P. / Merz, S. / Bracher, A. / Meyners, C. / Krewald, V. / Hausch, F. | ||||||
![]() | ![]() Title: Picomolar FKBP inhibitors enabled by a single water-displacing methyl group in bicyclic [4.3.1] aza-amides. Authors: Kolos, J.M. / Pomplun, S. / Jung, S. / Riess, B. / Purder, P.L. / Voll, A.M. / Merz, S. / Gnatzy, M. / Geiger, T.M. / Quist-Lokken, I. / Jatzlau, J. / Knaus, P. / Holien, T. / Bracher, A. / ...Authors: Kolos, J.M. / Pomplun, S. / Jung, S. / Riess, B. / Purder, P.L. / Voll, A.M. / Merz, S. / Gnatzy, M. / Geiger, T.M. / Quist-Lokken, I. / Jatzlau, J. / Knaus, P. / Holien, T. / Bracher, A. / Meyners, C. / Czodrowski, P. / Krewald, V. / Hausch, F. #1: ![]() Title: Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90. Authors: Bracher, A. / Kozany, C. / Thost, A.K. / Hausch, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 136.7 KB | Display | ![]() |
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PDB format | ![]() | 106.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 882.6 KB | Display | ![]() |
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Full document | ![]() | 886.4 KB | Display | |
Data in XML | ![]() | 11.7 KB | Display | |
Data in CIF | ![]() | 17.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7apqC ![]() 7apsC ![]() 7aptC ![]() 3o5qS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 14026.077 Da / Num. of mol.: 1 / Fragment: Fk1 domain Mutation: additional N-terminal sequence GAP, cloning artefact, mutation A19T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-RSB / ( |
#3: Water | ChemComp-HOH / |
Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.24 % / Mosaicity: 0.04 ° |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 36 % PEG-3350, 0.2 M NH4-acetate and 0.1 M HEPES-NaOH pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 26, 2015 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.72933 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 0.89→41.91 Å / Num. obs: 91415 / % possible obs: 89.5 % / Redundancy: 7.2 % / CC1/2: 0.995 / Rmerge(I) obs: 0.114 / Rpim(I) all: 0.035 / Rrim(I) all: 0.119 / Net I/σ(I): 13.7 / Num. measured all: 659976 / Scaling rejects: 9 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdbid 3O5Q Resolution: 0.89→30 Å / Cor.coef. Fo:Fc: 0.978 / Cor.coef. Fo:Fc free: 0.972 / SU B: 0.299 / SU ML: 0.008 / SU R Cruickshank DPI: 0.0161 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.016 / ESU R Free: 0.017 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 121.22 Å2 / Biso mean: 12.731 Å2 / Biso min: 4.75 Å2
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Refinement step | Cycle: final / Resolution: 0.89→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 0.89→0.913 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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